ArticleMolecular biology reports2011
Soluble expression, purification, and characterization of recombinant human flotillin-2 (reggie-1) in Escherichia coli.
Article in Molecular biology reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- A standardized set of pNX vectors for enhanced soluble expression of recombinant proteins in E. coli using small fusion tags.Microbial cell factories · 2025Article
- Recent advances in microbial fermentation for the production of leghemoglobin.World journal of microbiology & biotechnology · 2025Review
- Biotechnological production of the angiotensin-converting enzyme inhibitory dipeptide isoleucine-tryptophan.Engineering in life sciences · 2018Article
- Identification of Novel Raft Marker Protein, FlotP in Bacillus anthracis.Frontiers in microbiology · 2016Article
- Soluble expression and purification of Brucella cell surface protein (BCSP31) of Brucella melitensis and preparation of anti-BCSP31 monoclonal antibodies.Molecular biology reports · 2012Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
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Abstract
Large scale production of recombinant human flotillin-2 (reggie-1) is desirable for structural and biochemical studies. However, as the major lipid rafts specific hydrophobic protein, flotillin-2 was difficult to be expressed as soluble and functional form in prokaryotic system. In this study, we first cloned and expressed human flotillin-2 in Escherichia coli with five different fusion tags: poly-histidine, glutathione S-transferase (GST), thioredoxin (TRX), N-Utilization substance (NusA) and maltose binding protein (MBP). We screened the expression level and solubility of the five flotillin-2 fusion proteins, the best MBP tagged flotillin-2 was then large scale produced. The optimized purification procedure included two steps of chromatography: Ni-NTA affinity chromatography and anion exchange chromatography. The typical yield was 36.0 mg soluble and functional recombinant flotillin-2 from 1 L of culture medium with purity above 97%. The activity of recombinant flotillin-2 was verified by pull-down assay with flotillin-1, showing that the purified recombinant flotillin-2 can specifically interact with flotillin-1. The circular dichroism (CD) spectroscopy showed that recombinant flotillin-2 had a very stable secondary structure dominated by α-helix, β-turn and random structure.
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